메뉴 건너뛰기




Volumn 42, Issue 4, 2014, Pages 2708-2724

Identification of truncated forms of U1 snRNA reveals a novel RNA degradation pathway during snRNP biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

7 METHYLGUANOSINE; GUANOSINE; PROTEIN SM; RNA; SMALL NUCLEAR RIBONUCLEOPROTEIN; SURVIVAL MOTOR NEURON PROTEIN;

EID: 84895805892     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt1271     Document Type: Article
Times cited : (25)

References (52)
  • 1
    • 56649117675 scopus 로고    scopus 로고
    • The assembly of a spliceosomal small nuclear ribonucleoprotein particle
    • Patel, S.B. and Bellini, M. (2008) The assembly of a spliceosomal small nuclear ribonucleoprotein particle. Nucleic Acids Res., 36, 6482-6493.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6482-6493
    • Patel, S.B.1    Bellini, M.2
  • 2
    • 0023047717 scopus 로고
    • Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding
    • Mattaj, I.W. (1986) Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding. Cell, 46, 905-911.
    • (1986) Cell , vol.46 , pp. 905-911
    • Mattaj, I.W.1
  • 3
    • 0036809734 scopus 로고    scopus 로고
    • SMN-mediated assembly of RNPs: A complex story
    • Meister, G., Eggert, C. and Fischer, U. (2002) SMN-mediated assembly of RNPs: a complex story. Trends Cell Biol., 12, 472-478.
    • (2002) Trends Cell Biol. , vol.12 , pp. 472-478
    • Meister, G.1    Eggert, C.2    Fischer, U.3
  • 4
    • 0030928716 scopus 로고    scopus 로고
    • The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis
    • Fischer, U., Liu, Q. and Dreyfuss, G. (1997) The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis. Cell, 90, 1023-1029.
    • (1997) Cell , vol.90 , pp. 1023-1029
    • Fischer, U.1    Liu, Q.2    Dreyfuss, G.3
  • 5
    • 77952575677 scopus 로고    scopus 로고
    • Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis
    • Yong, J., Kasim, M., Bachorik, J.L., Wan, L. and Dreyfuss, G. (2010) Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis. Mol. Cell, 38, 551-562.
    • (2010) Mol. Cell , vol.38 , pp. 551-562
    • Yong, J.1    Kasim, M.2    Bachorik, J.L.3    Wan, L.4    Dreyfuss, G.5
  • 6
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl, M.C., Will, C.L. and Luhrmann, R. (2009) The spliceosome: design principles of a dynamic RNP machine. Cell, 136, 701-718.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 7
    • 45249106162 scopus 로고    scopus 로고
    • Spinal muscular atrophy
    • Lunn, M.R. and Wang, C.H. (2008) Spinal muscular atrophy. Lancet, 371, 2120-2133.
    • (2008) Lancet , vol.371 , pp. 2120-2133
    • Lunn, M.R.1    Wang, C.H.2
  • 8
    • 84862139693 scopus 로고    scopus 로고
    • Spliceosomal small nuclear ribonucleoprotein biogenesis defects and motor neuron selectivity in spinal muscular atrophy
    • Workman, E., Kolb, S.J. and Battle, D.J. (2012) Spliceosomal small nuclear ribonucleoprotein biogenesis defects and motor neuron selectivity in spinal muscular atrophy. Brain Res., 1462, 93-99.
    • (2012) Brain Res. , vol.1462 , pp. 93-99
    • Workman, E.1    Kolb, S.J.2    Battle, D.J.3
  • 9
    • 67651083390 scopus 로고    scopus 로고
    • Spinal muscular atrophy: Why do low levels of survival motor neuron protein make motor neurons sick?
    • Burghes, A.H. and Beattie, C.E. (2009) Spinal muscular atrophy: why do low levels of survival motor neuron protein make motor neurons sick? Nat. Rev. Neurosci., 10, 597-609.
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 597-609
    • Burghes, A.H.1    Beattie, C.E.2
  • 10
    • 2242443509 scopus 로고    scopus 로고
    • Essential role for the SMN complex in the specificity of snRNP assembly
    • Pellizzoni, L., Yong, J. and Dreyfuss, G. (2002) Essential role for the SMN complex in the specificity of snRNP assembly. Science, 298, 1775-1779.
    • (2002) Science , vol.298 , pp. 1775-1779
    • Pellizzoni, L.1    Yong, J.2    Dreyfuss, G.3
  • 11
    • 0036500546 scopus 로고    scopus 로고
    • Sequence-specific interaction of U1 snRNA with the SMN complex
    • Yong, J., Pellizzoni, L. and Dreyfuss, G. (2002) Sequence-specific interaction of U1 snRNA with the SMN complex. EMBO J., 21, 1188-1196.
    • (2002) EMBO J. , vol.21 , pp. 1188-1196
    • Yong, J.1    Pellizzoni, L.2    Dreyfuss, G.3
  • 12
    • 2142819496 scopus 로고    scopus 로고
    • Why do cells need an assembly machine for RNA-protein complexes?
    • Yong, J., Wan, L. and Dreyfuss, G. (2004) Why do cells need an assembly machine for RNA-protein complexes? Trends Cell Biol., 14, 226-232.
    • (2004) Trends Cell Biol. , vol.14 , pp. 226-232
    • Yong, J.1    Wan, L.2    Dreyfuss, G.3
  • 13
    • 66149121109 scopus 로고    scopus 로고
    • Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains
    • Lau, C.K., Bachorik, J.L. and Dreyfuss, G. (2009) Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains. Nat. Struct. Mol. Biol., 16, 486-491.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 486-491
    • Lau, C.K.1    Bachorik, J.L.2    Dreyfuss, G.3
  • 14
    • 79961137129 scopus 로고    scopus 로고
    • Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly
    • Zhang, R., So, B.R., Li, P., Yong, J., Glisovic, T., Wan, L. and Dreyfuss, G. (2011) Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly. Cell, 146, 384-395.
    • (2011) Cell , vol.146 , pp. 384-395
    • Zhang, R.1    So, B.R.2    Li, P.3    Yong, J.4    Glisovic, T.5    Wan, L.6    Dreyfuss, G.7
  • 17
    • 44449137369 scopus 로고    scopus 로고
    • Deciphering the assembly pathway of Sm-class U snRNPs
    • Neuenkirchen, N., Chari, A. and Fischer, U. (2008) Deciphering the assembly pathway of Sm-class U snRNPs. FEBS Lett., 582, 1997-2003.
    • (2008) FEBS Lett. , vol.582 , pp. 1997-2003
    • Neuenkirchen, N.1    Chari, A.2    Fischer, U.3
  • 18
    • 0033613150 scopus 로고    scopus 로고
    • SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins
    • Pellizzoni, L., Charroux, B. and Dreyfuss, G. (1999) SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins. Proc. Natl Acad. Sci. USA, 96, 11167-11172.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11167-11172
    • Pellizzoni, L.1    Charroux, B.2    Dreyfuss, G.3
  • 19
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms, H., Meheus, L., de Brabandere, V., Fischer, U. and Luhrmann, R. (2001) Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA, 7, 1531-1542.
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 20
    • 0037459239 scopus 로고    scopus 로고
    • High-resolution X-ray and NMR structures of the SMN Tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues
    • Sprangers, R., Groves, M.R., Sinning, I. and Sattler, M. (2003) High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues. J. Mol. Biol., 327, 507-520.
    • (2003) J. Mol. Biol. , vol.327 , pp. 507-520
    • Sprangers, R.1    Groves, M.R.2    Sinning, I.3    Sattler, M.4
  • 21
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • Friesen, W.J., Massenet, S., Paushkin, S., Wyce, A. and Dreyfuss, G. (2001) SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell, 7, 1111-1117.
    • (2001) Mol. Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 23
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • Meister, G., Eggert, C., Buhler, D., Brahms, H., Kambach, C. and Fischer, U. (2001) Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr. Biol., 11, 1990-1994.
    • (2001) Curr. Biol. , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 24
    • 33646377172 scopus 로고    scopus 로고
    • Gemin8 is a novel component of the survival motor neuron complex and functions in small nuclear ribonucleoprotein assembly
    • Carissimi, C., Saieva, L., Baccon, J., Chiarella, P., Maiolica, A., Sawyer, A., Rappsilber, J. and Pellizzoni, L. (2006) Gemin8 is a novel component of the survival motor neuron complex and functions in small nuclear ribonucleoprotein assembly. J. Biol. Chem., 281, 8126-8134.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8126-8134
    • Carissimi, C.1    Saieva, L.2    Baccon, J.3    Chiarella, P.4    Maiolica, A.5    Sawyer, A.6    Rappsilber, J.7    Pellizzoni, L.8
  • 25
    • 20444382808 scopus 로고    scopus 로고
    • The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex has an Sm protein-like structure
    • Ma, Y., Dostie, J., Dreyfuss, G. and Van Duyne, G.D. (2005) The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex has an Sm protein-like structure. Structure, 13, 883-892.
    • (2005) Structure , vol.13 , pp. 883-892
    • Ma, Y.1    Dostie, J.2    Dreyfuss, G.3    Van Duyne, G.D.4
  • 26
    • 67649782140 scopus 로고    scopus 로고
    • Role of survival motor neuron complex components in small nuclear ribonucleoprotein assembly
    • Ogawa, C., Usui, K., Ito, F., Itoh, M., Hayashizaki, Y. and Suzuki, H. (2009) Role of survival motor neuron complex components in small nuclear ribonucleoprotein assembly. J. Biol. Chem., 284, 14609-14617.
    • (2009) J. Biol. Chem. , vol.284 , pp. 14609-14617
    • Ogawa, C.1    Usui, K.2    Ito, F.3    Itoh, M.4    Hayashizaki, Y.5    Suzuki, H.6
  • 27
    • 33846010157 scopus 로고    scopus 로고
    • Gemin8 is required for the architecture and function of the survival motor neuron complex
    • Carissimi, C., Saieva, L., Gabanella, F. and Pellizzoni, L. (2006) Gemin8 is required for the architecture and function of the survival motor neuron complex. J. Biol. Chem., 281, 37009-37016.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37009-37016
    • Carissimi, C.1    Saieva, L.2    Gabanella, F.3    Pellizzoni, L.4
  • 28
    • 34047100275 scopus 로고    scopus 로고
    • A comprehensive interaction map of the human survival of motor neuron (SMN) complex
    • Otter, S., Grimmler, M., Neuenkirchen, N., Chari, A., Sickmann, A. and Fischer, U. (2007) A comprehensive interaction map of the human survival of motor neuron (SMN) complex. J. Biol. Chem., 282, 5825-5833.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5825-5833
    • Otter, S.1    Grimmler, M.2    Neuenkirchen, N.3    Chari, A.4    Sickmann, A.5    Fischer, U.6
  • 29
    • 34547461601 scopus 로고    scopus 로고
    • U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies
    • Liu, J.L. and Gall, J.G. (2007) U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies. Proc. Natl Acad. Sci. USA, 104, 11655-11659.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11655-11659
    • Liu, J.L.1    Gall, J.G.2
  • 30
    • 67649873112 scopus 로고    scopus 로고
    • The spinal muscular atrophy protein SMN affects Drosophila germline nuclear organization through the U body-P body pathway
    • Lee, L., Davies, S.E. and Liu, J.L. (2009) The spinal muscular atrophy protein SMN affects Drosophila germline nuclear organization through the U body-P body pathway. Dev. Biol., 332, 142-155.
    • (2009) Dev. Biol. , vol.332 , pp. 142-155
    • Lee, L.1    Davies, S.E.2    Liu, J.L.3
  • 31
  • 32
    • 75649120041 scopus 로고    scopus 로고
    • An analytical platform for mass spectrometry-based identification and chemical analysis of RNA in ribonucleoprotein complexes
    • Taoka, M., Yamauchi, Y., Nobe, Y., Masaki, S., Nakayama, H., Ishikawa, H., Takahashi, N. and Isobe, T. (2009) An analytical platform for mass spectrometry-based identification and chemical analysis of RNA in ribonucleoprotein complexes. Nucleic Acids Res., 37, e140.
    • (2009) Nucleic Acids Res. , vol.37
    • Taoka, M.1    Yamauchi, Y.2    Nobe, Y.3    Masaki, S.4    Nakayama, H.5    Ishikawa, H.6    Takahashi, N.7    Isobe, T.8
  • 34
    • 82955249329 scopus 로고    scopus 로고
    • Informatics for mass spectrometry-based RNA analysis
    • Nakayama, H., Takahashi, N. and Isobe, T. (2011) Informatics for mass spectrometry-based RNA analysis. Mass Spectrom. Rev., 30, 1000-1012.
    • (2011) Mass Spectrom. Rev. , vol.30 , pp. 1000-1012
    • Nakayama, H.1    Takahashi, N.2    Isobe, T.3
  • 35
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • Pomeranz Krummel, D.A., Oubridge, C., Leung, A.K., Li, J. and Nagai, K. (2009) Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Nature, 458, 475-480.
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 36
    • 34249053165 scopus 로고    scopus 로고
    • RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation
    • Hogg, J.R. and Collins, K. (2007) RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation. RNA, 13, 868-880.
    • (2007) RNA , vol.13 , pp. 868-880
    • Hogg, J.R.1    Collins, K.2
  • 37
    • 30544439063 scopus 로고    scopus 로고
    • Nuclear export and cytoplasmic processing of precursors to the 40S ribosomal subunits in mammalian cells
    • Rouquette, J., Choesmel, V. and Gleizes, P.E. (2005) Nuclear export and cytoplasmic processing of precursors to the 40S ribosomal subunits in mammalian cells. EMBO J., 24, 2862-2872.
    • (2005) EMBO J. , vol.24 , pp. 2862-2872
    • Rouquette, J.1    Choesmel, V.2    Gleizes, P.E.3
  • 40
    • 0035887042 scopus 로고    scopus 로고
    • Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein
    • Hebert, M.D., Szymczyk, P.W., Shpargel, K.B. and Matera, A.G. (2001) Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein. Genes Dev., 15, 2720-2729.
    • (2001) Genes Dev. , vol.15 , pp. 2720-2729
    • Hebert, M.D.1    Szymczyk, P.W.2    Shpargel, K.B.3    Matera, A.G.4
  • 41
    • 0002425959 scopus 로고    scopus 로고
    • Posttranscriptional modifications in the U small nuclear RNAs
    • Grosjean, H. and Benne, R. (eds), ASM Press, Washington, DC
    • Massenet, S., Mougin, A. and Branlant, C. (1998) Posttranscriptional modifications in the U small nuclear RNAs. In: Grosjean, H. and Benne, R. (eds), The Modification and Editing of RNA. ASM Press, Washington, DC, pp. 201-227.
    • (1998) The Modification and Editing of RNA , pp. 201-227
    • Massenet, S.1    Mougin, A.2    Branlant, C.3
  • 42
    • 0034646512 scopus 로고    scopus 로고
    • PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
    • Ohno, M., Segref, A., Bachi, A., Wilm, M. and Mattaj, I.W. (2000) PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation. Cell, 101, 187-198.
    • (2000) Cell , vol.101 , pp. 187-198
    • Ohno, M.1    Segref, A.2    Bachi, A.3    Wilm, M.4    Mattaj, I.W.5
  • 44
    • 49349110521 scopus 로고    scopus 로고
    • Expression of human snRNA genes from beginning to end
    • Egloff, S., O'Reilly, D. and Murphy, S. (2008) Expression of human snRNA genes from beginning to end. Biochem. Soc. Trans., 36, 590-594.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 590-594
    • Egloff, S.1    O'Reilly, D.2    Murphy, S.3
  • 45
    • 65249168677 scopus 로고    scopus 로고
    • A role for ubiquitin in the clearance of nonfunctional rRNAs
    • Fujii, K., Kitabatake, M., Sakata, T., Miyata, A. and Ohno, M. (2009) A role for ubiquitin in the clearance of nonfunctional rRNAs. Genes Dev., 23, 963-974.
    • (2009) Genes Dev. , vol.23 , pp. 963-974
    • Fujii, K.1    Kitabatake, M.2    Sakata, T.3    Miyata, A.4    Ohno, M.5
  • 46
    • 26844493853 scopus 로고    scopus 로고
    • Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II
    • Baillat, D., Hakimi, M.A., Naar, A.M., Shilatifard, A., Cooch, N. and Shiekhattar, R. (2005) Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II. Cell, 123, 265-276.
    • (2005) Cell , vol.123 , pp. 265-276
    • Baillat, D.1    Hakimi, M.A.2    Naar, A.M.3    Shilatifard, A.4    Cooch, N.5    Shiekhattar, R.6
  • 47
    • 79951715071 scopus 로고    scopus 로고
    • Regulation of alternative splicing by the core spliceosomal machinery
    • Saltzman, A.L., Pan, Q. and Blencowe, B.J. (2011) Regulation of alternative splicing by the core spliceosomal machinery. Genes Dev., 25, 373-384.
    • (2011) Genes Dev. , vol.25 , pp. 373-384
    • Saltzman, A.L.1    Pan, Q.2    Blencowe, B.J.3
  • 48
    • 78649847070 scopus 로고    scopus 로고
    • U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation
    • Kaida, D., Berg, M.G., Younis, I., Kasim, M., Singh, L.N., Wan, L. and Dreyfuss, G. (2010) U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation. Nature, 468, 664-668.
    • (2010) Nature , vol.468 , pp. 664-668
    • Kaida, D.1    Berg, M.G.2    Younis, I.3    Kasim, M.4    Singh, L.N.5    Wan, L.6    Dreyfuss, G.7
  • 51
    • 0037106283 scopus 로고    scopus 로고
    • A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics
    • Natsume, T., Yamauchi, Y., Nakayama, H., Shinkawa, T., Yanagida, M., Takahashi, N. and Isobe, T. (2002) A direct nanoflow liquid chromatography- tandem mass spectrometry system for interaction proteomics. Anal. Chem., 74, 4725-4733.
    • (2002) Anal. Chem. , vol.74 , pp. 4725-4733
    • Natsume, T.1    Yamauchi, Y.2    Nakayama, H.3    Shinkawa, T.4    Yanagida, M.5    Takahashi, N.6    Isobe, T.7
  • 52
    • 44049123270 scopus 로고
    • Tandem mass spectrometry of small multiply charged oligonucleotides
    • McLuckey, S.A., Van Berkel, G.J. and Glish, G.L. (1992) Tandem mass spectrometry of small multiply charged oligonucleotides. J. Am. Soc. Mass Spectrom., 3, 60-70.
    • (1992) J. Am. Soc. Mass Spectrom. , vol.3 , pp. 60-70
    • McLuckey, S.A.1    Van Berkel, G.J.2    Glish, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.